1hmc: Difference between revisions

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 <StructureSection load='1hmc' size='340' side='right'caption='[[1hmc]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1hmc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HMC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1hmc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HMC FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hmc OCA], [https://pdbe.org/1hmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hmc RCSB], [https://www.ebi.ac.uk/pdbsum/1hmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hmc ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hmc OCA], [https://pdbe.org/1hmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hmc RCSB], [https://www.ebi.ac.uk/pdbsum/1hmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hmc ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[https://www.uniprot.org/uniprot/CSF1_HUMAN CSF1_HUMAN]] Note=Aberrant expression of CSF1 or CSF1R can promote cancer cell proliferation, invasion and formation of metastases. Overexpression of CSF1 or CSF1R is observed in a significant percentage of breast, ovarian, prostate, and endometrial cancers.<ref>PMID:16337366</ref> <ref>PMID:19934330</ref>   Note=Aberrant expression of CSF1 or CSF1R may play a role in inflammatory diseases, such as rheumatoid arthritis, glomerulonephritis, atherosclerosis, and allograft rejection.<ref>PMID:16337366</ref> <ref>PMID:19934330</ref>
+[https://www.uniprot.org/uniprot/CSF1_HUMAN CSF1_HUMAN] Note=Aberrant expression of CSF1 or CSF1R can promote cancer cell proliferation, invasion and formation of metastases. Overexpression of CSF1 or CSF1R is observed in a significant percentage of breast, ovarian, prostate, and endometrial cancers.<ref>PMID:16337366</ref> <ref>PMID:19934330</ref>   Note=Aberrant expression of CSF1 or CSF1R may play a role in inflammatory diseases, such as rheumatoid arthritis, glomerulonephritis, atherosclerosis, and allograft rejection.<ref>PMID:16337366</ref> <ref>PMID:19934330</ref>
 == Function ==
-[[https://www.uniprot.org/uniprot/CSF1_HUMAN CSF1_HUMAN]] Cytokine that plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. Promotes the release of proinflammatory chemokines, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone development. Required for normal male and female fertility. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration. Plays a role in lipoprotein clearance.<ref>PMID:16337366</ref> <ref>PMID:19934330</ref> <ref>PMID:20829061</ref> <ref>PMID:20504948</ref>
+[https://www.uniprot.org/uniprot/CSF1_HUMAN CSF1_HUMAN] Cytokine that plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. Promotes the release of proinflammatory chemokines, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone development. Required for normal male and female fertility. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration. Plays a role in lipoprotein clearance.<ref>PMID:16337366</ref> <ref>PMID:19934330</ref> <ref>PMID:20829061</ref> <ref>PMID:20504948</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hmc ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Macrophage colony-stimulating factor (M-CSF) triggers the development of cells of the monocyte-macrophage lineage and has a variety of stimulatory effects on mature cells of this class. The biologically active form of M-CSF is a disulfide-linked dimer that activates an intrinsic tyrosine kinase activity on the M-CSF receptor by inducing dimerization of the receptor molecules. The structure of a recombinant human M-CSF dimer, determined at 2.5 angstroms by x-ray crystallography, contains two bundles of four alpha helices laid end-to-end, with an interchain disulfide bond. Individual monomers of M-CSF show a close structural similarity to the cytokines granulocyte-macrophage colony-stimulating factor and human growth hormone. Both of these cytokines are monomeric in their active form, and their specific receptors lack intrinsic tyrosine kinase activity. The similarity of these structures suggests that the receptor binding determinants for all three cytokines may be similar.
-Three-dimensional structure of dimeric human recombinant macrophage colony-stimulating factor.,Pandit J, Bohm A, Jancarik J, Halenbeck R, Koths K, Kim SH Science. 1992 Nov 20;258(5086):1358-62. PMID:1455231<ref>PMID:1455231</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1hmc" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Bohm, A]]
+[[Category: Bohm A]]
-[[Category: Halenbeck, R]]
+[[Category: Halenbeck R]]
-[[Category: Jancarik, J]]
+[[Category: Jancarik J]]
-[[Category: Kim, S H]]
+[[Category: Kim S-H]]
-[[Category: Koths, K]]
+[[Category: Koths K]]
-[[Category: Pandit, J]]
+[[Category: Pandit J]]
-[[Category: Macrophage colony stimulating factor]]